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Conserved domains on  [gi|25149598|ref|NP_495206|]
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Charged multivesicular body protein 4b [Caenorhabditis elegans]

Protein Classification

Snf7 family protein( domain architecture ID 10505749)

Snf7 family protein may be involved in protein sorting and transport from the endosome to the vacuole/lysosome

Gene Ontology:  GO:0007034
PubMed:  32875105

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
38-202 2.28e-44

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


:

Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 146.61  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598    38 EAIGNLRDAEELLIKKQEYFELRIEQEVESAKKY-MKTNKKMALAALRKKKHYEQELSRIDGVLTKLEAQRTALENVGMH 116
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLaKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598   117 NEVIDVLGKTTETLKKEHAKMDIDKVHDLMDEIADGLAMSEELNEAISAPIGDVA--DEDELMQELQELQDNVADlSTTT 194
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADeeDEEELDAELDALLDEIGD-EESV 159

                  ....*...
gi 25149598   195 KLPDVPAT 202
Cdd:pfam03357 160 ELPSAPSG 167
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
38-202 2.28e-44

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 146.61  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598    38 EAIGNLRDAEELLIKKQEYFELRIEQEVESAKKY-MKTNKKMALAALRKKKHYEQELSRIDGVLTKLEAQRTALENVGMH 116
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLaKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598   117 NEVIDVLGKTTETLKKEHAKMDIDKVHDLMDEIADGLAMSEELNEAISAPIGDVA--DEDELMQELQELQDNVADlSTTT 194
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADeeDEEELDAELDALLDEIGD-EESV 159

                  ....*...
gi 25149598   195 KLPDVPAT 202
Cdd:pfam03357 160 ELPSAPSG 167
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
28-210 6.90e-11

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 59.83  E-value: 6.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598   28 SRKRKAPTADEAIGNLRDAEELLIKKQEyfelRIEQEVESAKKYMKTNKKM--------ALAALRKKKHYEQELSRIDGV 99
Cdd:PTZ00464   8 KNKTPKPTLEDASKRIGGRSEVVDARIN----KIDAELMKLKEQIQRTRGMtqsrhkqrAMQLLQQKRMYQNQQDMMMQQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598  100 LTKLEAQRTALENVGMHNEVIDVLGKTTETLKKEHAKMDIDKVHDLMDEIADGLAMSEELNEAISAPIG--DVADEDELM 177
Cdd:PTZ00464  84 QFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDvpDDIDEDEML 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 25149598  178 QELQELQ---DNVADLSTTTKLPDVPAT-LPEAPSGE 210
Cdd:PTZ00464 164 GELDALDfdmEKEADASYLADALAVPGTkLPDVPTDE 200
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
38-202 2.28e-44

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 146.61  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598    38 EAIGNLRDAEELLIKKQEYFELRIEQEVESAKKY-MKTNKKMALAALRKKKHYEQELSRIDGVLTKLEAQRTALENVGMH 116
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLaKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598   117 NEVIDVLGKTTETLKKEHAKMDIDKVHDLMDEIADGLAMSEELNEAISAPIGDVA--DEDELMQELQELQDNVADlSTTT 194
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADeeDEEELDAELDALLDEIGD-EESV 159

                  ....*...
gi 25149598   195 KLPDVPAT 202
Cdd:pfam03357 160 ELPSAPSG 167
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
28-210 6.90e-11

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 59.83  E-value: 6.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598   28 SRKRKAPTADEAIGNLRDAEELLIKKQEyfelRIEQEVESAKKYMKTNKKM--------ALAALRKKKHYEQELSRIDGV 99
Cdd:PTZ00464   8 KNKTPKPTLEDASKRIGGRSEVVDARIN----KIDAELMKLKEQIQRTRGMtqsrhkqrAMQLLQQKRMYQNQQDMMMQQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598  100 LTKLEAQRTALENVGMHNEVIDVLGKTTETLKKEHAKMDIDKVHDLMDEIADGLAMSEELNEAISAPIG--DVADEDELM 177
Cdd:PTZ00464  84 QFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDvpDDIDEDEML 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 25149598  178 QELQELQ---DNVADLSTTTKLPDVPAT-LPEAPSGE 210
Cdd:PTZ00464 164 GELDALDfdmEKEADASYLADALAVPGTkLPDVPTDE 200
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
28-185 9.91e-11

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 58.97  E-value: 9.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149598   28 SRKRKAPTADEAIGNLRDAEELLIKKQEYFELRIEQ-EVESAKKYMKTNKKMALAALRKKKHYEQELSRIDGVLTKLEAQ 106
Cdd:PTZ00446  17 NKKKNNDEIYKAILKNREAIDALEKKQVQVEKKIKQlEIEAKQKVEQNQMSNAKILLKRKKLYEQEIENILNNRLTLEDN 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25149598  107 RTALENVGMHNEVIDVLGKTTETLKKEHAKMDIDKVHDLMDEIADGLAMSEELNEAISAPIGDVADEDELMQELQELQD 185
Cdd:PTZ00446  97 MINLENMHLHKIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALSFNLLNNVDDDEIDKELDLLKE 175
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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